RPOB_PASMU
ID RPOB_PASMU Reviewed; 1342 AA.
AC Q9CK91;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=PM1737;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AE004439; AAK03821.1; -; Genomic_DNA.
DR RefSeq; WP_010907308.1; NC_002663.1.
DR AlphaFoldDB; Q9CK91; -.
DR SMR; Q9CK91; -.
DR STRING; 747.DR93_617; -.
DR EnsemblBacteria; AAK03821; AAK03821; PM1737.
DR KEGG; pmu:PM1737; -.
DR PATRIC; fig|272843.6.peg.1759; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047933"
SQ SEQUENCE 1342 AA; 149567 MW; 1B60A6441A6C3C6C CRC64;
MVYSYTEKKR IRKDFGKRPQ VLNVPYLLTI QLDSFDKFIQ RDPEGQQGLE AAFRSVFPIV
SNNGNTELQY VSYQLGEPVF DVRECQIRGT TYAAPLRVKL RLVSYDKDAA PGTIKDIKEQ
EVYMGEIPLM TDNGTFVING TERVIVSQLH RSPGVFFDSD KGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDNLYARIDR RRKLPATIIL RALNYTTEQI LDIFFDKVVF EISNNKLLMT
LVPERLRGET ATFDIEANGK VYVERGRRIT ARHIRALEKD QITQVEVPTE YIVGKVAAKD
YVDLESGEIV CPANMEISLE MLAKLAQAGY KTIETLFTND LDYGPYISET LRVDPSNDRL
SALVEIYRMM RPGEPPTKEA AEGLFDNLFF SSDRYDLSAV GRMKFNRSLG IDEETGSGIL
SNDDIIGVMK KLIEIRNGRG EVDDIDHLGN RRIRSVGEMA ENQFRIGLVR VERAVKERLS
LGDLDAVTPQ DLINAKPISA AVKEFFGSSQ LSQFMDQNNP LSEVTHKRRI SALGPGGLTR
ERAGFEVRDV HATHYGRVCP IETPEGPNIG LINSLSVYAR TNDYGFLETP YRKVVNGQVT
EEIEYLSAIE EGKYVIAQAN SNLDEELRFT DAFVTCRGEH GESGLYRPDE IHYMDVSTQQ
VVSVAAALIP FLEHDDANRA LMGANMQRQA VPTLRADKPL VGTGIEKAVA VDSGVTVIAK
RGGMVQYVDA SRIVVKVNED ETIPGEAGID IYNLVKYTRS NQNTCINQIP CVSLGEPIGR
GEVLADGPST DLGELALGQN MRVAFMPWNG YNFEDSMLVS ERVVQEDRFT TIHIQELSCV
ARDTKLGSEE ITADIPNVGE AALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNSVSGTVI DVQVFTRDGV EKDKRALEIE EMQLKQAKKD
LVEELEILEA GLFTRVRSLL IAGGFDAKNL DKLDRTKWLE QSLSDEAQQN QLEQLAEQYE
ELRKEFERKL EVQRGKIIQG DDLAPGVLKV VKVYLAVKRQ IQPGDKMAGR HGNKGVISKI
NPVEDMPYDE NGQPVDIVLN PLGVPSRMNI GQILETHLGL AAKGIGDKIN AMIKQQQDVA
KLREYMQKAY DLGHGSQKVD LSTFSDEEVM RLAQNLRKGL PLATPVFDGA HESEIKGLLE
LGGLPTSGQI TLFDGRTGEK FERPVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTKMYKNIVG GTHQMDPGTP
ESFNVIMKEI RSLGINIDLD ED